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8HJ5

Cryo-EM structure of Gq-coupled MRGPRX1 bound with Compound-16

Functional Information from GO Data
ChainGOidnamespacecontents
A0003924molecular_functionGTPase activity
A0005525molecular_functionGTP binding
A0007165biological_processsignal transduction
A0007186biological_processG protein-coupled receptor signaling pathway
A0019001molecular_functionguanyl nucleotide binding
A0031683molecular_functionG-protein beta/gamma-subunit complex binding
B0001750cellular_componentphotoreceptor outer segment
B0003924molecular_functionGTPase activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005765cellular_componentlysosomal membrane
B0005829cellular_componentcytosol
B0005834cellular_componentheterotrimeric G-protein complex
B0005886cellular_componentplasma membrane
B0007165biological_processsignal transduction
B0007186biological_processG protein-coupled receptor signaling pathway
B0007191biological_processadenylate cyclase-activating dopamine receptor signaling pathway
B0007200biological_processphospholipase C-activating G protein-coupled receptor signaling pathway
B0007213biological_processG protein-coupled acetylcholine receptor signaling pathway
B0007265biological_processRas protein signal transduction
B0008283biological_processcell population proliferation
B0016020cellular_componentmembrane
B0030159molecular_functionsignaling receptor complex adaptor activity
B0044877molecular_functionprotein-containing complex binding
B0045202cellular_componentsynapse
B0050909biological_processsensory perception of taste
B0051020molecular_functionGTPase binding
B0060041biological_processretina development in camera-type eye
B0070062cellular_componentextracellular exosome
B0071380biological_processcellular response to prostaglandin E stimulus
B0071870biological_processcellular response to catecholamine stimulus
B0097381cellular_componentphotoreceptor disc membrane
B1903561cellular_componentextracellular vesicle
D0005515molecular_functionprotein binding
D0005834cellular_componentheterotrimeric G-protein complex
D0005886cellular_componentplasma membrane
D0007165biological_processsignal transduction
D0007186biological_processG protein-coupled receptor signaling pathway
D0007191biological_processadenylate cyclase-activating dopamine receptor signaling pathway
D0016020cellular_componentmembrane
D0031681molecular_functionG-protein beta-subunit binding
D0045202cellular_componentsynapse
D0048144biological_processfibroblast proliferation
D0070062cellular_componentextracellular exosome
D0071380biological_processcellular response to prostaglandin E stimulus
D0071870biological_processcellular response to catecholamine stimulus
F0004888molecular_functiontransmembrane signaling receptor activity
F0004930molecular_functionG protein-coupled receptor activity
F0005506molecular_functioniron ion binding
F0005886cellular_componentplasma membrane
F0006953biological_processacute-phase response
F0007165biological_processsignal transduction
F0007166biological_processcell surface receptor signaling pathway
F0007186biological_processG protein-coupled receptor signaling pathway
F0009055molecular_functionelectron transfer activity
F0009986cellular_componentcell surface
F0016020cellular_componentmembrane
F0020037molecular_functionheme binding
F0022900biological_processelectron transport chain
F0042597cellular_componentperiplasmic space
F0046872molecular_functionmetal ion binding
F1902349biological_processresponse to chloroquine
Functional Information from PROSITE/UniProt
site_idPS00237
Number of Residues17
DetailsG_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. AGLsFLSAVSTERCLsV
ChainResidueDetails
FALA108-VAL124

site_idPS00678
Number of Residues15
DetailsWD_REPEATS_1 Trp-Asp (WD) repeats signature. LVSAsqDgKLIIWDS
ChainResidueDetails
BLEU91-SER105
BILE178-ILE192
BLEU306-ALA320
BVAL348-GLY362

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: axial binding residue
ChainResidueDetails
FTRP-99
FILE-4

site_idSWS_FT_FI2
Number of Residues59
DetailsTOPO_DOM: Extracellular => ECO:0000255
ChainResidueDetails
FMET1-THR31
FSER89-LYS96
FSER166-ASP177
FHIS243-HIS254

site_idSWS_FT_FI3
Number of Residues20
DetailsTRANSMEM: Helical; Name=1 => ECO:0000255
ChainResidueDetails
FVAL32-LEU52

site_idSWS_FT_FI4
Number of Residues108
DetailsTOPO_DOM: Cytoplasmic => ECO:0000255
ChainResidueDetails
FGLY53-ASN67
FTHR118-VAL144
FLEU199-THR221
FGLY276-GLN322

site_idSWS_FT_FI5
Number of Residues20
DetailsTRANSMEM: Helical; Name=2 => ECO:0000255
ChainResidueDetails
FLEU68-ILE88

site_idSWS_FT_FI6
Number of Residues20
DetailsTRANSMEM: Helical; Name=3 => ECO:0000255
ChainResidueDetails
FILE97-SER117

site_idSWS_FT_FI7
Number of Residues20
DetailsTRANSMEM: Helical; Name=4 => ECO:0000255
ChainResidueDetails
FLEU145-PHE165

site_idSWS_FT_FI8
Number of Residues20
DetailsTRANSMEM: Helical; Name=5 => ECO:0000255
ChainResidueDetails
FPHE178-LEU198

site_idSWS_FT_FI9
Number of Residues20
DetailsTRANSMEM: Helical; Name=6 => ECO:0000255
ChainResidueDetails
FVAL222-ILE242

site_idSWS_FT_FI10
Number of Residues20
DetailsTRANSMEM: Helical; Name=7 => ECO:0000255
ChainResidueDetails
FLEU255-VAL275

site_idSWS_FT_FI11
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
FASN16

237735

PDB entries from 2025-06-18

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